PMID- 9353121
OWN - NLM
STAT- MEDLINE
DCOM- 19971121
LR  - 20151119
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 389
IP  - 6654
DP  - 1997 Oct 30
TI  - The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1.
PG  - 974-8
AB  - Spinocerebellar ataxia type 1 (SCA1) is an autosomal dominant neurodegenerative 
      disorder characterized by ataxia, progressive motor deterioration, and loss of 
      cerebellar Purkinje cells. SCA1 belongs to a growing group of neurodegenerative 
      disorders caused by expansion of CAG repeats, which encode glutamine. Although 
      the proteins containing these repeats are widely expressed, the neurodegeneration 
      in SCA1 and other polyglutamine diseases selectively involves a few neuronal 
      subtypes. The mechanism(s) underlying this neuronal specificity is unknown. Here 
      we show that the cerebellar leucine-rich acidic nuclear protein (LANP) interacts 
      with ataxin-1, the SCA1 gene product. LANP is expressed predominantly in Purkinje 
      cells, the primary site of pathology in SCA1. The interaction between LANP and 
      ataxin-1 is significantly stronger when the number of glutamines is increased. 
      Immunofluorescence studies demonstrate that both LANP and ataxin-1 colocalize in 
      nuclear matrix-associated subnuclear structures. The features of the interaction 
      between ataxin-1 and LANP, their spatial and temporal patterns of expression, and 
      the colocalization studies indicate that cerebellar LANP is involved in the 
      pathogenesis of SCA1.
FAU - Matilla, A
AU  - Matilla A
AD  - Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA.
FAU - Koshy, B T
AU  - Koshy BT
FAU - Cummings, C J
AU  - Cummings CJ
FAU - Isobe, T
AU  - Isobe T
FAU - Orr, H T
AU  - Orr HT
FAU - Zoghbi, H Y
AU  - Zoghbi HY
LA  - eng
SI  - GENBANK/AF022957
SI  - GENBANK/AF025684
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (ATXN1 protein, human)
RN  - 0 (Anp32a protein, rat)
RN  - 0 (Ataxin-1)
RN  - 0 (Ataxins)
RN  - 0 (Atxn1 protein, mouse)
RN  - 0 (Atxn1 protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Nuclear Proteins)
RN  - 0RH81L854J (Glutamine)
SB  - IM
EIN - Nature 1998 Feb 19;391(6669):818
MH  - Animals
MH  - Ataxin-1
MH  - Ataxins
MH  - Binding Sites
MH  - COS Cells
MH  - Cell Nucleus/metabolism
MH  - Cerebellum/cytology/*metabolism
MH  - Cloning, Molecular
MH  - Glutamine/metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Mice
MH  - Microscopy, Confocal
MH  - Mutation
MH  - Nerve Tissue Proteins/genetics/*metabolism
MH  - Neuropeptides/*metabolism
MH  - Nuclear Matrix/metabolism
MH  - Nuclear Proteins/genetics/*metabolism
MH  - Purkinje Cells/metabolism
MH  - Rats
MH  - Saccharomyces cerevisiae
MH  - Spinocerebellar Degenerations/metabolism
EDAT- 1997/11/14 00:00
MHDA- 2001/03/23 10:01
CRDT- 1997/11/14 00:00
PHST- 1997/11/14 00:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1997/11/14 00:00 [entrez]
AID - 10.1038/40159 [doi]
PST - ppublish
SO  - Nature. 1997 Oct 30;389(6654):974-8. doi: 10.1038/40159.